PMID:11884747
| Citation |
Jormakka, M, Törnroth, S, Byrne, B and Iwata, S (2002) Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295:1863-8 |
|---|---|
| Abstract |
The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined at 1.6 angstroms. The structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 angstroms through the enzyme. The menaquinone reduction site associated with a possible proton pathway was also characterized. This structure provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes. |
| Links |
PubMed Online version:10.1126/science.1068186 |
| Keywords |
Binding Sites; Catalysis; Catalytic Domain; Cell Membrane/enzymology; Crystallography, X-Ray; Electron Transport; Escherichia coli/enzymology; Formate Dehydrogenases/chemistry; Formate Dehydrogenases/metabolism; Formates/metabolism; Guanine Nucleotides/chemistry; Guanine Nucleotides/metabolism; Hydrogen Bonding; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/metabolism; Membrane Potentials; Models, Molecular; Nitrate Reductases/chemistry; Nitrate Reductases/metabolism; Oxidation-Reduction; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Subunits; Proton-Motive Force; Protons; Pterins/chemistry; Pterins/metabolism; Vitamin K 2/chemistry; Vitamin K 2/metabolism |
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